A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria.

Erythrina poeppigiana belongs to Fabaceae family (subfamily Papillionoideae) and is commonly found in tropical and subtropical regions in Brazil. Herein, we described the purification and characterization of a new Kunitz-type inhibitor, obtained from E. poeppigiana seeds (EpTI).

Adepamycin: design, synthesis and biological properties of a new peptide with antimicrobial properties.

Antimicrobial peptides (AMP) are molecules with a broad spectrum of activities that have been identified in most living organisms. In addition, synthetic AMPs designed from natural polypeptides have been largely investigated. Here, we designed a novel AMP using the amino acid sequence of a plant trypsin inhibitor from Adenanthera pavonina seeds (ApTI) as a template.

Novel Peptidase Kunitz Inhibitor from Platypodium elegans Seeds Is Active against Spodoptera frugiperda Larvae.

A novel Kunitz-type inhibitor from Platypodium elegans seeds (PeTI) was purified and characterized. The mass spectrometry analyses of PeTI indicated an intact mass of 19 701 Da and a partial sequence homologous to Kunitz inhibitors. PeTI was purified by ion exchange and affinity chromatographies.

Antibiotic combinations for controlling colistin-resistant Enterobacter cloacae.

Enterobacter cloacae is a Gram-negative bacterium associated with high morbidity and mortality in intensive care patients due to its resistance to multiple antibiotics. Currently, therapy against multi-resistant bacteria consists of using colistin, in spite of its toxic effects at higher concentrations. In this context, colistin-resistant E.

Antimicrobial Activity of ILTI, a Kunitz-Type Trypsin Inhibitor from Inga laurina (SW.) Willd.

Over the last few years, a growing number of proteinase inhibitors have been isolated from plants and particularly from seeds and have shown antimicrobial activity. A 20,000 Da serine peptidase inhibitor, named ILTI, was isolated from Inga laurina seeds and showed potent inhibitory enzymatic activity against trypsin. The aim of this study was to determine the effects of ILTI on the growth of pathogenic and non-pathogenic microorganisms.

Understanding bacterial resistance to antimicrobial peptides: From the surface to deep inside.

Resistant bacterial infections are a major health problem in many parts of the world. The major commercial antibiotic classes often fail to combat common bacteria. Although antimicrobial peptides are able to control bacterial infections by interfering with microbial metabolism and physiological processes in several ways, a large number of cases of resistance to antibiotic peptide classes have also been reported.

Screening of antimicrobials from Caribbean sea animals and isolation of bactericidal proteins from the littoral mollusk Cenchritis muricatus.

Marine organisms represent approximately half of the world's biodiversity by virtue of the sea being an immense reservoir of bioactive molecules. Here, antimicrobial crude extract activities of different marine invertebrates from the Caribbean Sea were evaluated. One of the most active, crude extracts was that marine snail Cenchritis muricatus, it was capable of totally inhibiting the development of Staphylococcus aureus and also showed a growth inhibition of 95.

Deciphering the magainin resistance process of Escherichia coli strains in light of the cytosolic proteome.

Antimicrobial peptides (AMPs) are effective antibiotic agents commonly found in plants, animals, and microorganisms, and they have been suggested as the future of antimicrobial chemotherapies. It is vital to understand the molecular details that define the mechanism of action of resistance to AMPs for a rational planning of the next antibiotic generation and also to shed some light on the complex AMP mechanism of action. Here, the antibiotic resistance of Escherichia coli ATCC 8739 to magainin I was evaluated in the cytosolic subproteome.

Bactericidal activity identified in 2S Albumin from sesame seeds and in silico studies of structure-function relations.

Pathogenic bacteria constitute an important cause of hospital-acquired infections. However, the misuse of available bactericidal agents has led to the appearance of antibiotic-resistant strains. Thus, efforts to seek new antimicrobials with different action mechanisms would have an enormous impact.

Comparative analyses of different surfactants on matrix-assisted laser desorption/ionization mass spectrometry peptide analysis.

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been extensively used for proteomics and peptidomics analysis. Nevertheless, these analyses, when focused on low molecular mass proteins, show some limitation due to background interference from surfactant ions. Surfactants are routinely used as a solubilizing or denaturing agents for proteins and peptides.

Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water.

Infections caused by pathogenic bacteria could cause an expressive negative impact on human health. A significant enhance in resistance to commercial antibiotics has been observed in all kinds of pathogenic bacteria. In order to find novel approaches to control such common infections, a wide number of defense peptides with bactericidal properties have been characterized.

Susceptibility of human pathogenic bacteria to antimicrobial peptides from sesame kernels.

Hospital infection caused by Gram-negative bacteria is a serious and common problem, especially in developing countries. Aiming to reduce these infections, this report focuses on the identification and characterization of novel antimicrobial peptides from sesame (Sesamum indicum) kernel meals. Thus, sesame flour was extracted and precipitated with ammonium sulfate (100%).